Chlorine in PDB 1d3j: N-Terminal Domain Core Methionine Mutation

All present enzymatic activity of N-Terminal Domain Core Methionine Mutation:
3.2.1.17;

The structure of N-Terminal Domain Core Methionine Mutation, PDB code: 1d3j was solved by N.C.Gassner, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.97
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.110, 61.110, 97.330, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the N-Terminal Domain Core Methionine Mutation (pdb code 1d3j). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the N-Terminal Domain Core Methionine Mutation, PDB code: 1d3j:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the N-Terminal Domain Core Methionine Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of N-Terminal Domain Core Methionine Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:30.4 occ:1.00 O A:HOH209 3.0 35.8 1.0 N A:ASN144 3.2 6.9 1.0 N A:ARG145 3.4 13.1 1.0 C A:THR142 3.4 21.1 1.0 CA A:THR142 3.5 7.8 1.0 CB A:THR142 3.5 21.7 1.0 CB A:ASN144 3.7 9.9 1.0 O A:THR142 3.7 12.1 1.0 N A:PRO143 3.8 19.5 1.0 CA A:ASN144 3.8 8.8 1.0 CB A:ARG145 4.0 13.2 1.0 C A:ASN144 4.1 23.0 1.0 C A:PRO143 4.1 12.9 1.0 CG2 A:THR142 4.2 15.9 1.0 CD A:PRO143 4.2 12.5 1.0 CA A:ARG145 4.3 14.9 1.0 CA A:PRO143 4.5 14.1 1.0 CG A:ASN144 4.6 31.6 1.0 OG1 A:THR142 4.7 18.1 1.0 ND2 A:ASN144 4.7 29.4 1.0 O A:HOH230 4.8 36.5 1.0 N A:THR142 4.9 8.8 1.0 CG A:PRO143 5.0 13.8 1.0

Chlorine binding site 2 out of 2 in the N-Terminal Domain Core Methionine Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of N-Terminal Domain Core Methionine Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:44.5 occ:0.50 O A:HOH215 3.0 29.8 1.0 O A:HOH182 3.6 26.1 1.0 O A:HOH200 3.7 45.6 1.0 CB A:ALA49 4.0 14.0 1.0 O A:HOH282 4.2 37.1 1.0 CE1 A:HIS31 4.3 16.0 1.0 O A:HOH246 4.4 68.1 1.0 CA A:ALA49 4.4 20.0 1.0 NE2 A:HIS31 4.5 14.8 1.0 CE A:MET66 4.6 55.0 1.0 NE2 A:GLN69 4.7 19.2 1.0 O A:HOH202 4.7 56.6 1.0

N.C.Gassner, B.W.Matthews. Use of Differentially Substituted Selenomethionine Proteins in X-Ray Structure Determination. Acta Crystallogr.,Sect.D V. 55 1967 1999.
ISSN: ISSN 0907-4449
PubMed: 10666571
DOI: 10.1006/JMBI.1999.3220